dbPTM

EF2_SCHPO - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	EF2_SCHPO
UniProt AC	O14460
Protein Name	Elongation factor 2
Gene Name	eft201
Organism	Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
Sequence Length	842
Subcellular Localization	Cytoplasm.
Protein Description	Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome (By similarity)..
Protein Sequence	MVAFTPEEVRNLMGKPSNVRNMSVIAHVDHGKSTLTDSLVQKAGIISAAKAGDARFMDTRADEQERGVTIKSTAISLFAEMTDDDMKDMKEPADGTDFLVNLIDSPGHVDFSSEVTAALRVTDGALVVVDTIEGVCVQTETVLRQALGERIRPVVVVNKVDRALLELQISQEELYQNFARVVESVNVVISTYYDKVLGDCQVFPDKGTVAFASGLHGWAFTVRQFANRYAKKFGIDRNKMMQRLWGENYFNPKTKKWSKSATDANGNSNQRAFNMFILDPIYRIFDAVMNSRKDEVFTLLSKLEVTIKPDEKELEGKALLKVVMRKFLPAADALMEMIVLHLPSPKTAQQYRAETLYEGPMDDECAVGIRNCDANAPLMIYVSKMVPTSDRGRFYAFGRVFSGTVRSGLKVRIQGPNYVPGKKDDLFIKAIQRTVLMMGSRIEPIEDCPAGNIIGLVGVDQFLVKSGTLTTSEVAHNMKVMKFSVSPVVQVAVEVKNGNDLPKLVEGLKRLSKSDPCVLCTTSESGEHIVAGAGELHLEICLKDLQEDHAGIPLKISPPVVSYRESVSEPSSMTALSKSPNKHNRIFMTAEPMSEELSVAIETGHVNPRDDFKVRARIMADEFGWDVTDARKIWCFGPDTTGANVVVDQTKAVAYLNEIKDSVVAAFAWASKEGPMFEENLRSCRFNILDVVLHADAIHRGGGQIIPTARRVVYASTLLASPIIQEPVFLVEIQVSENAMGGIYSVLNKKRGHVFSEEQRVGTPLYNIKAYLPVNESFGFTGELRQATAGQAFPQLVFDHWSPMSGDPLDPTSKPGQIVCEARKRKGLKENVPDYTEYYDRL

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
33	Phosphorylation	AHVDHGKSTLTDSLV EEEECCCCCCCHHHH	32.99	25720772
34	Phosphorylation	HVDHGKSTLTDSLVQ EEECCCCCCCHHHHH	36.84	28889911
36	Phosphorylation	DHGKSTLTDSLVQKA ECCCCCCCHHHHHHH	24.51	25720772
38	Phosphorylation	GKSTLTDSLVQKAGI CCCCCCHHHHHHHCH	25.79	28889911
59	Phosphorylation	GDARFMDTRADEQER CCCCCCCCCCCHHHC	18.90	25720772
73	Phosphorylation	RGVTIKSTAISLFAE CCCEEHHHHHHHHHH	24.02	25720772
82	Phosphorylation	ISLFAEMTDDDMKDM HHHHHHCCCCHHHHC	27.99	21712547
402	Phosphorylation	YAFGRVFSGTVRSGL EEEEEEEECCCCCCC	30.60	25720772
466	Phosphorylation	VDQFLVKSGTLTTSE ECEEEEECCCEEHHH	29.54	25720772
468	Phosphorylation	QFLVKSGTLTTSEVA EEEEECCCEEHHHHH	28.20	27738172
557	Phosphorylation	AGIPLKISPPVVSYR CCCCCEECCCEEECC	22.89	25720772
566	Phosphorylation	PVVSYRESVSEPSSM CEEECCCCCCCCCCC	23.19	29996109
568	Phosphorylation	VSYRESVSEPSSMTA EECCCCCCCCCCCCC	53.74	28889911
571	Phosphorylation	RESVSEPSSMTALSK CCCCCCCCCCCCCCC	28.79	25720772
572	Phosphorylation	ESVSEPSSMTALSKS CCCCCCCCCCCCCCC	30.76	25720772
574	Phosphorylation	VSEPSSMTALSKSPN CCCCCCCCCCCCCCC	26.79	28889911
577	Phosphorylation	PSSMTALSKSPNKHN CCCCCCCCCCCCCCC	28.73	29996109
579	Phosphorylation	SMTALSKSPNKHNRI CCCCCCCCCCCCCCE	30.26	29996109
699	Diphthamide	VLHADAIHRGGGQII HHCCHHHHHCCCCCC	24.85	-
699	Amidation	VLHADAIHRGGGQII HHCCHHHHHCCCCCC	24.85	-

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Modified Location	Modified Residue	Modification	Type of Upstream Proteins	Gene Name of Upstream Proteins	UniProt AC of Upstream Proteins	Sources
Oops, there are no upstream regulatory protein records of EF2_SCHPO !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of EF2_SCHPO !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location	Modification	Variant Position (Distance <= 10)	Residue Change	SAP	Related Disease	Reference
Oops, there are no SNP-PTM records of EF2_SCHPO !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of EF2_SCHPO !!

Drug and Disease Associations

Kegg Drug
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of EF2_SCHPO

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Phosphoproteome analysis of fission yeast."; Wilson-Grady J.T., Villen J., Gygi S.P.; J. Proteome Res. 7:1088-1097(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-568 AND THR-574, ANDMASS SPECTROMETRY.	18257517 [Abstract]